Research workbench
AlphaFold monomer V2.0 prediction for bifunctional NAD(P)H-hydrate repair enzyme nnr (D1BAA5)
Analyse AlphaFold monomer V2.0 prediction for bifunctional NAD(P)H-hydrate repair… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- D1BAA5
- Type
- protein
- Length
- 512 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- Molecule
- Bifunctional NAD(P)H-hydrate repair enzyme nnr
- UniProt
- D1BAA5
- Pockets
- 3 · best druggability 0.59
Structure
1 distinct chain · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional NAD(P)H-hydrate repair enzyme nnr | protein | 512 | 46% helix, 18% strand | D1BAA5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.59 | 0.81 | 28 | empty |
| 2 | 257 | 0.55 | 0.77 | 33 | empty |
| 3 | 67 | 0.34 | 0.76 | 14 | empty |
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt D1BAA5
- Elsewhere: UniProt D1BAA5 · AlphaFold DB D1BAA5
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